ID A0A364K7F2_9BACL Unreviewed; 732 AA.
AC A0A364K7F2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=DNA topoisomerase 3 {ECO:0000256|HAMAP-Rule:MF_00953};
DE EC=5.6.2.1 {ECO:0000256|HAMAP-Rule:MF_00953};
DE AltName: Full=DNA topoisomerase III {ECO:0000256|HAMAP-Rule:MF_00953};
GN Name=topB {ECO:0000256|HAMAP-Rule:MF_00953};
GN ORFNames=DL897_04300 {ECO:0000313|EMBL:RAL26226.1};
OS Thermoflavimicrobium daqui.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Thermoflavimicrobium.
OX NCBI_TaxID=2137476 {ECO:0000313|EMBL:RAL26226.1, ECO:0000313|Proteomes:UP000251213};
RN [1] {ECO:0000313|EMBL:RAL26226.1, ECO:0000313|Proteomes:UP000251213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBKL4.011 {ECO:0000313|EMBL:RAL26226.1,
RC ECO:0000313|Proteomes:UP000251213};
RA Wang X., Zhou H.;
RT "Thermoflavimicrobium daqus sp. nov., a thermophilic microbe isolated from
RT Moutai-flavour Daqu.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RAL26226.1, ECO:0000313|Proteomes:UP000251213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBKL4.011 {ECO:0000313|EMBL:RAL26226.1,
RC ECO:0000313|Proteomes:UP000251213};
RA Zhirakovskaya E.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Releases the supercoiling and torsional tension of DNA, which
CC is introduced during the DNA replication and transcription, by
CC transiently cleaving and rejoining one strand of the DNA duplex.
CC Introduces a single-strand break via transesterification at a target
CC site in duplex DNA. The scissile phosphodiester is attacked by the
CC catalytic tyrosine of the enzyme, resulting in the formation of a DNA-
CC (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH
CC DNA strand. The free DNA strand then undergoes passage around the
CC unbroken strand, thus removing DNA supercoils. Finally, in the
CC religation step, the DNA 3'-OH attacks the covalent intermediate to
CC expel the active-site tyrosine and restore the DNA phosphodiester
CC backbone. {ECO:0000256|HAMAP-Rule:MF_00953}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC passage and rejoining.; EC=5.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000213, ECO:0000256|HAMAP-
CC Rule:MF_00953};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00953};
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00009446, ECO:0000256|HAMAP-Rule:MF_00953}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00953}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RAL26226.1}.
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DR EMBL; QJKK01000002; RAL26226.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364K7F2; -.
DR OrthoDB; 9803554at2; -.
DR Proteomes; UP000251213; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR CDD; cd00186; TOP1Ac; 1.
DR CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR Gene3D; 3.40.50.140; -; 1.
DR Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1.
DR Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1.
DR Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 1.
DR HAMAP; MF_00953; Topoisom_3_prok; 1.
DR InterPro; IPR000380; Topo_IA.
DR InterPro; IPR003601; Topo_IA_2.
DR InterPro; IPR023406; Topo_IA_AS.
DR InterPro; IPR013497; Topo_IA_cen.
DR InterPro; IPR013824; Topo_IA_cen_sub1.
DR InterPro; IPR013825; Topo_IA_cen_sub2.
DR InterPro; IPR013826; Topo_IA_cen_sub3.
DR InterPro; IPR023405; Topo_IA_core_domain.
DR InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR InterPro; IPR005738; TopoIII.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034144; TOPRIM_TopoIII.
DR NCBIfam; TIGR01056; topB; 1.
DR PANTHER; PTHR11390:SF21; DNA TOPOISOMERASE 3-ALPHA; 1.
DR PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR PRINTS; PR00417; PRTPISMRASEI.
DR SMART; SM00437; TOP1Ac; 1.
DR SMART; SM00436; TOP1Bc; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00953};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00953};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00953};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00953};
KW Reference proteome {ECO:0000313|Proteomes:UP000251213};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00953}.
FT DOMAIN 3..136
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 187..192
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT ACT_SITE 311
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT SITE 61
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT SITE 168
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT SITE 176
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
FT SITE 313
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00953"
SQ SEQUENCE 732 AA; 84247 MW; BE4EA1151607E300 CRC64;
MGKTVVLAEK PSVGKDIAKV LHCHQQKNGY YEGDRYIVTW AFGHLVTLAD PERYKEAYKT
WRLEDLPILP DRLKLVVIKK TSRQFQQVKT LMTRPDIKQI IIATDAGREG ELVARWIIEK
TKVKKPIQRL WISSVTDKAI KEGFQRLRDG KQYENLYRSA VARAEADWIV GINATRALTC
KHNAQLSCGR VQTPTLSMIA EREMEIRNFQ SKPFYGIEVT ADNLLKLTWQ NRKTNDGRIF
SKEKCEQLLT KLKNQDGIIT EVKKTKKKRF APALYDLTEL QREANQRFGY SAKETLSILQ
KLYEYHKVLT YPRTDSRYLS SDIVGTLKDR IEACRVGPYR TLASQAMKHL RPNKHFIDDR
KVSDHHAIIP TEEPVILDKL SLKERKIYDL VVRRFLAVMY PPFEYEQTIV QVEIAGETFI
ARGKVILAQG FKQVYEDYPE EEEKGEGIKE QILPKLERGS HLKIGSIVQT EGKTQPPEPF
TEGTLIAAME NPVRFMKRER NDLIKTLGET GGLGTVATRA DIIEKLFATF LIEKKGKYIY
ITSKGKQLLD LVPEELKSPA LTAEWEQKLA DIAKGKLNQD IFIKEMRKYA KDVVQEIKET
TKAFKHDNLS TKKCPDCGKR LLEVKSKKGQ MLVCQDRTCG YRKGVARVTN ARCPECRKKL
ELRGEGEGRI FVCGCGYREK YASFEKRKEK EKKGKVSKKE ITKYLKQQNQ LQEQGNPALK
EALAKLFQKD GR
//